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High-resolution influenza 2009 H1N1 endonuclease bound to 4-(1H- imidazol-1-YL)PHENOL

Analyse High-resolution influenza 2009 H1N1 endonuclease bound to 4-(1H… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4M5R
Type: protein
Length: 201 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Polymerase pa
UniProt: F0TRT1
Ligands: MSR, MN, SO4
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Polymerase pa	protein	201	48% helix, 15% strand	F0TRT1

Ligands and binding sites

MSR · 4-(1H-imidazol-1-yl)phenol · ligand · 2 copies · chains A
MN · Manganese (II) ion · metal · 4 copies · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	512	0.66	0.77	39	MN, MSR, EDO

Compared structures

4M5R · High-resolution influenza 2009 H1N1 endonuclease bound to 4-(1H-IMIDAZOL-1-YL)PHENOL · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt F0TRT1
Elsewhere: RCSB PDB 4M5R · PDBe 4M5R · UniProt F0TRT1

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